1H NMR studies of the binding of bacteriophage-M13-encoded gene-5 protein to oligo(deoxyadenylic acid)s of varying length.

1H NMR studies of the binding of bacteriophage-M13-encoded gene-5 protein to oligo(deoxyadenylic acid)s of varying length.
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噬菌体 M13 编码的基因 5 蛋白与不同长度的寡聚(脱氧腺苷酸)结合的 1 H NMR 研究。

DOI:
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发表时间:
1982
期刊:
European Journal of Biochemistry
影响因子:
--
通讯作者:
C. W. Hilbers
C. W. Hilbers
中科院分区:
--
文献类型:
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作者:
N. Alma;B. Harmsen;J. V. van Boom;G. A. van der Marel;C. W. Hilbers

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用2 ~ 16个核苷酸的寡核苷酸滴定基因-5蛋白,并在360 MHz记录~ 1H NMR谱,研究了基因-5蛋白与寡核苷酸的结合。为了获得关于蛋白质结合模式的信息,通过进行光谱模拟来分析光谱的芳香族部分,从在500 MHz下从核Overhausfer增强获得的分配开始[阿尔马,N. C. M.,Harmsen,B. J.M.,船体,W. E、货车德马雷尔,G.,货车Boom,J.H.,和Hilbers,C. W.(1981)Biochemistry,20,4419-4428]。基因-5蛋白质与(dA)8、(dA)12和(dA)16的复合物的1H NMR光谱似乎是相同的,除了线宽的差异。具有较小寡核苷酸(dA)2、(dA)3和(dA)4的复合物的1H NMR光谱彼此不同,并且与从具有较长寡核苷酸的复合物获得的光谱不同。然而,所有寡核苷酸的结合基本上影响相同的芳香族残基,即两个酪氨酸和一个苯丙氨酸。在蛋白质-寡核苷酸复合物中,一个蛋白质单体覆盖三个核苷酸残基,与蛋白质-多核苷酸复合物中发现的1:4的化学计量相反。发现与寡核苷酸的结合是协同的和离子强度依赖性的,但远低于与多核苷酸的结合。
The binding of gene-5 protein to oligo(deoxyadenylic acid)s varying in length from 2 to 16 nucleotides has been studied by titrating the protein with the oligonucleotides and recording the 1H NMR spectra at 360 MHz. To obtain information about the mode of binding of the protein the aromatic parts of the spectra have been analysed by performing spectral simulations, starting from the assignments obtained from nuclear Overhausfer enhancements at 500 MHz [Alma, N. C. M., Harmsen, B. J. M., Hull, W. E., Van der Marel, G., Van Boom, J.H., and Hilbers, C. W. (1981) Biochemistry, 20, 4419-4428]. The 1H NMR spectra of the complexes of gene-5 protein with (dA)8, (dA)12 and (dA)16 appear to be identical except for differences in linewidth. The 1H NMR spectra of the complexes with the smaller oligonucleotides (dA)2, (dA)3 and (dA)4 differ from each other and from the spectra obtained from the complexes with longer oligonucleotides. However, binding of all oligonucleotides basically influences the same aromatic residues, namely two tyrosines and one phenylalanine. In the protein-oligonucleotide complexes, one protein monomer covers three nucleotide residues, in contrast to the stoichiometry of 1:4 found for protein-polynucleotide complexes. It was found that the binding to oligonucleotides is cooperative and ionic-strength-dependent but far less so than found for the binding to polynucleotides.
DOI: 10.1016/0022-2836(81)90335-1
发表时间: 1981-01-01
影响因子: 5.6
作者:
KOWALCZYKOWSKI, SC;LONBERG, N;VONHIPPEL, PH
通讯作者: VONHIPPEL, PH
DOI: 10.1016/0022-2836(81)90390-9
发表时间: 1981
影响因子: 5.6
作者:
Torbet,J;Gray,DM;Gray,CW;Marvin,DA;Siegrist,H
通讯作者: Siegrist,H